Differentiation of human skeletal muscle cells in culture: maturation as indicated by titin and desmin striation |
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Authors: | Peter F M van der Ven Gert Schaart Paul H K Jap Rob C A Sengers Ad M Stadhouders Francs C S Ramaekers |
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Institution: | (1) Department of Cell Biology and Histology, University of Nijmegen, PB Box 9101, 6500 HB Nijmegen, The Netherlands;(2) Department of Molecular Cell Biology and Genetics, University of Limburg, Maastricht, The Netherlands;(3) Department of Pediatrics, University of Nijmegen, The Netherlands |
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Abstract: | Summary This report describes a phenotyping study of differentiating human skeletal muscle cells in tissue culture. Satellite cells (adult myoblasts), isolated from biopsy material, showed a proliferative behaviour in high-nutrition medium, but fused to form myotubes when grown in low-nutrition medium. The expression and structural organization of the intermediate filament proteins desmin and vimentin as well as the sarcomeric constituents -actin, -actinin, nebulin, myosin and especially titin during myofibrillogenesis in vitro, were studied by means of indirect immunofluorescence assays. The proliferating myoblasts contained both desmin and vimentin, -actinin and the filamentous form of actin. Shortly after the change of medium, expression of titin, sarcomeric myosin and skeletal muscle -actin was found in mononuclear cells in a diffuse, filamentous (titin, myosin, -actin) or punctate (titin, myosin) pattern. Four to 10 days after the medium change, mature myotubes showed desmin, titin, -actinin, nebulin, sarcomeric myosin and actin cross-striations, while vimentin was no longer detected. We conclude that human skeletal muscle cell cultures are an appropriate model system to study the molecular basis of myofibrillogenesis. Especially the presence of desmin in a striated fashion points to a high degree of maturation of the muscle cell cultures. |
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Keywords: | Skeletal muscle cells Myofibrillogenesis Intermediate filaments Titin Nebulin Myosin -Actinin" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">-Actinin Human |
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